BMRB Entry 30442

Name: TFE-induced NMR structure of an antimicrobial peptide (EcDBS1R5) derived from a mercury transporter protein (MerP - Escherichia coli)
Published: 2018-11-09

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PDB ID: 6ct4
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30442
MolProbity Validation Chart

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

TFE-induced NMR structure of an antimicrobial peptide (EcDBS1R5) derived from a mercury transporter protein (MerP - Escherichia coli)

Deposition date:

2018-03-22

Original release date:

2018-11-09

Authors:

Cardoso, M.; Chan, L.; Candido, E.; Craik, D.; Franco, O.

Citation:

Citation: Cardoso, Marlon; Candido, Elizabete; Chan, Lai; Der Torossian Torres, Marcelo; Oshiro, Karen; Rezende, Samilla; Porto, William; Lu, Timothy; de la Fuente-Nunez, Cesar; Craik, David; Franco, Octavio. "A Computationally Designed Peptide Derived from Escherichia coli as a Potential Drug Template for Antibacterial and Antibiofilm Therapies" ACS Infect. Dis. 4, 1727-1736 (2018).
PubMed: 30346140

Assembly members:

Assembly members:
entity_1, polymer, 19 residues, 2152.794 Da.

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: PMKKLKLALRLAAKIAPVW

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1

Data type	Count
13C chemical shifts	65
15N chemical shifts	17
1H chemical shifts	162

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 19 residues - 2152.794 Da.

1

PRO

MET

LYS

LEU

LYS

LEU

ALA

LEU

ARG

2

LEU

ALA

LYS

ILE

ALA

PRO

VAL

TRP

Samples:

sample_1: EcDBS1R5 1 mM; TFE 30%; H2O 60%; D2O 10%; DSS 10%

sample_conditions_1: pH: 4.3; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H TOCSY	sample_1	anisotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	anisotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	anisotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	anisotropic	sample_conditions_1

Software:

CcpNMR, CCPN - chemical shift assignment, peak picking

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

CYANA, Guntert, Mumenthaler and Wuthrich - data analysis

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure calculation

NMR spectrometers:

Bruker Avance 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks